References
- Alvarez ME, White CB, Gregory J, et al. (1995). Phevalin, a new calpain inhibitor, from a Streptomyces sp. J Antibiot 48:1165–7
- Alvarez ME, Houck DR, White CB, et al. (1994). Isolation and structure elucidation of two new calpain inhibitors from Streptomyces griseus. J Antibiot 47:1195–201
- Aoyagi T, Hatsu M, Imada C, et al. (1992). Pyrizinostatin: a new inhibitor of pyroglutamyl peptidase. J Antibiot 45:1795–6
- Arrieta JM, Herndl GJ. (2001). Assessing the diversity of marine bacterial β-glucosidases by capillary electrophoresis zymography. Appl Environ Microbiol 67:4896–900
- Asano N. (2003). Glycosidase inhibitors: update and perspectives on practical use. Glycobiology 13:93R–104R
- Asano N, Nash RJ, Molyneux RJ, Fleet GW. (2000). Sugar-mimic glycosidase inhibitors: natural occurrence, biological activity and prospects for therapeutic application. Tetrahedron Asymme. 11:1645–80
- Banks BJ, Haxell MA, Lunn G et al. (2007). Treatment of rumen acidosis with α-amylase inhibitors, European Patent, EP1157696
- Birari RB, Bhutani KK. (2007). Pancreatic lipase inhibitors from natural sources: unexplored potential. Drug Discov Today 12:879–89
- Bo-Linn GW, Santa Ana CA, Morawski SG, Fordtran JS. (1982). Starch blockers – their effect on calorie absorption from a high-starch meal. New Engl J Med 307:1413–16
- Borges de Melo E, da Silveira Gomes A, Carvalho I. (2006). α- and β-Glucosidase inhibitors: chemical structure and biological activity. Tetrahedron 62:10277–302
- Bush K, Henry PR, Souser-Woehleke M, et al. (1984). Phenacein – an angiotensin-converting enzyme inhibitor produced by a streptomycete. I. Taxonomy, fermentation and biological properties. J Antibiot 37:1308–12
- Demuth H-U. (1990). Recent developments in inhibiting cysteine and serine proteases. J Enzyme Inhibition Med Chem 3:249–78
- Donkor I. (2000). A survey of calpain inhibitors. Curr Med Chem 7:1171–88
- Donkor I, Sanders ML. (2001). Synthesis of a reported calpain inhibitor isolated from Streptomyces griseus. Bioorg Med Chem Lett 11:2647–9
- Floss HG. (1997). Natural products derived from unusual variants of the shikimate pathway. Nat Prod Rep 14:433–52
- Friedman LS, Peterson WL. (1998). Peptic ulcer and related disorders. In: Fauci AS, Braunwald E, Isselbacher JD, et al, eds. Harrison’s principles of internal medicine. New York: McGraw-Hill, 1597–610
- Ganesan S, Raja S, Sampathkumar P, et al. (2011). Isolation and screening of α-glucosidase enzyme inhibitor producing marine actinobacteria. Afr J Microbiol Res 5:3437–45
- Geng P, Qiu F, Zhu Y, Bai G. (2008). Four acarviosin-containing oligosaccharides identified from Streptomyces coelicoflavus ZG0656 are potent inhibitors of α-amylase. Carbohyd Res 343:882–92
- Geng P, Bai G, Shi Q, et al. (2009). Taxonomy of the Streptomyces strain ZG0656 that produces acarviostatin α-amylase inhibitors and analysis of their effects on blood glucose levels in mammalian systems. J Appl Microbiol 106:525–33
- Hadvary P, Sidler W, Meister W, et al. (1991). The lipase inhibitor tetrahydrolipstatin binds covalently to the putative active site serine of pancreatic lipase. J Biol Chem 266:2021–7
- Hall JE, Bhatta N, Adams JM, et al. (1991). Variable tolerance of the developing follicle and corpus luteum to gonadotropin-releasing hormone antagonist-induced gonadotropin withdrawal in the human. J Clin Endocr Metab 72:993–1000
- Hirayama K, Takahashi R, Akashi S, et al. (1987). Primary structure of Paim I, an alpha-amylase inhibitor from Streptomyces corchorushii, as determined by the combination of Edman degradation and fast atom bombardment mass spectrometry. Biochem 26:6483–8
- Holland D, Tronrud D, Pley H, et al. (1992). Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis. Biochem 31:11310–16
- Horovitz ZP (editor). (1981). Angiotensin converting enzyme inhibitors: mechanisms of action and clinical implications. Baltimore and Munich: Urban & Schwarzenberg
- Imada C. (2004). Enzyme inhibitors of marine microbial origin with pharmaceutical importance. Mar Biotechnol 6:193–8
- Imada C. (2005). Enzyme inhibitors and other bioactive compounds from marine actinomycetes. Antonie Van Leeuwenhoek 87:59–63
- Imada C, Okami Y. (1995). Characteristics of marine actinomycete isolated from a deep-sea sediment and production of beta-glucosidase inhibitor. J Mar Biotechnol 2:109–13
- Imada C, Sugimoto Y, Makimura T, et al. (2001). Isolation and characterization of tyrosinase inhibitor-producing microorganisms from marine environment. Fish Sci 67:1151–6
- Johnston PS, Lebovitz HE, Coniff RF, et al. (1998). Advantages of α-glucosidase inhibition as monotherapy in elderly type 2 diabetic patients. J Clin Endocr Metab 83:1515–22
- Kangouri K, Namiki S, Nagate T et al. (1980). Novel amylase inhibitors, US Patent, 41972921980
- Kido Y, Hamakado T, Yoshida T, et al. (1983). Isolation and characterization of ancovenin, a new inhibitor of angiotensin I converting enzyme, produced by actinomycetes. J Antibiot 36:1295–9
- Kim JH, Ryu YB, Kang NS, et al. (2006). Glycosidase inhibitory flavonoids from Sophora flavescens. Biol Pharm Bull 29:302–5
- Kodani S, Ohnishi-Kameyama M, Yoshida M, Ochi K. (2011). A new siderophore isolated from Streptomyces sp. TM-34 with potent inhibitory activity against angiotensin-converting enzyme. Eur J Org Chem 2011:3191–6
- Krowarsch D, Cierpicki T, Jelen F, Otlewski J. (2003). Canonical protein inhibitors of serine proteases. Cell Mol Life Sci 60:2427–44
- Kuehn L, Dahlmann B, Reinauer H. (1984). Identification of four distinct serine proteinase inhibitors in rat skeletal muscle. Biochem Biophys Res Commun 120:96–102
- Kunio Suetsuna, Nagatomo K, Doi K. (1994). Structure of α-amylase inhibitor produced by marine actinomycete and its lowering effects in vivo of glucose and lipid in blood. J Shimonoseki University Fisheries 42:171–83
- Lin G, Chattopadhyay D, Maki M, et al. (1997). Crystal structure of calcium bound domain VI of calpain at 1.9 Å resolution and its role in enzyme assembly, regulation, and inhibitor binding. Nature Structural Biol 4:539–47
- Lovejoy B, Cleasby A, Hassell AM, et al. (1994). Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor. Science 263:375–7
- Mahmud T, Tornus I, Egelkrout E, et al. (1999). Biosynthetic studies on the α-glucosidase inhibitor acarbose in Actinoplanes sp.: 2-epi-5-epi-valiolone is the direct precursor of the valienamine moiety. J Am Chem Soc 121:6973–83
- Manivasagan P, Venkatesan J, Sivakumar K, Kim S-K. (2013a). Actinobacterial melanins: current status and perspective for the future. World J Microbiol Biotechnol 1–14 . DOI 10. 1007/s11274-013-1352-y
- Manivasagan P, Venkatesan J, Sivakumar K, Kim S-K. (2013b). Marine actinobacterial metabolites: Current status and future perspectives. Microbiol Res 168:311–32
- Manivasagan P, Venkatesan J, Senthilkumar K, et al. (2013c). Isolation and characterization of biologically active melanin from Actinoalloteichus sp. MA-32. Int J Biol Macromol 58:263–74
- Meng P, Zhou X. (2012). α-Glucosidase inhibitory effect of a bioactivity guided fraction GIB-638 from Streptomyces fradiae PWH638. Med Chem Res 21:4422–9
- Meng P, Xie C, Geng P, et al. (2013). Inhibitory effect of components from Streptomyces species on α-glucosidase and α-amylase of different origin. Appl Biochem Microbiol 49:160–8
- Menon V, Rao M. (2012). Slow-tight binding inhibition of pepsin by an aspartic protease inhibitor from Streptomyces sp. MBR04. Int J Biol Macromol 51:165–74
- Misasa H, Matsui Y, Uehara H, et al. (1992). Tyrosinase inhibitors from Albatrellus confluens. Biosci Biotechnol Biochem 56:1660–1
- Mutoh M, Nakada N, Matsukuma S, et al. (1994). Panclicins, novel pancreatic lipase inhibitors. I. Taxonomy, fermentation, isolation and biological activity. J Antibiot 47:1369–75
- Oda K, Koyama T, Murao S. (1979). Purification and properties of a proteinaceous metallo-proteinase inhibitor from Streptomyces nigrescens TK-23. Biochim Biophys Acta Enzymol 571:147–56
- Ohno A, Tate S-i, Seeram SS, et al. (1998). NMR structure of the Streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23: another example of an ancestral βγ-crystallin precursor structure. J Mol Biol 282:421–33
- Ondetti MA, Rubin B, Cushman DW. (1977). Design of specific inhibitors of angiotensin-converting enzyme: new class of orally active antihypertensive agents. Science 196:441–4
- Otto H-H, Schirmeister T. (1997). Cysteine proteases and their inhibitors. Chem Rev 97:133–72
- Pandhare J, Zog K, Deshpande VV. (2002). Differential stabilities of alkaline protease inhibitors from actinomycetes: effect of various additives on thermostability. Bioresour Technol 84:165–9
- Pierpoint W. (1966). The enzymic oxidation of chlorogenic acid and some reactions of the quinone produced. Biochem J 98:567–80
- Powers JC, Harper JW. (1986). Inhibitors of metalloproteases. In: Barrett AJ, Salvesen G, eds. Proteinase inhibitors. Vol. 12. Amsterdam: Elsevier BV, 219–98
- Prasad C, Peterkofsky A. (1976). Demonstration of pyroglutamylpeptidase and amidase activities toward thyrotropin-releasing hormone in hamster hypothalamus extracts. J Biol Chem 251:3229–34
- Prashith Kekuda T, Shobha K, Onkarappa R. (2011). Pancreatic lipase inhibitory and cytotoxic potential of a Streptomyces species isolated from Western Ghat soil, Agumbe, Karnataka, India. Int J Pharmaceutical Biol Archive 2:932–7
- Priestley G (editor). (1993). An introduction to the skin and its diseases. In: Molecular aspects of dermatology. Vol. 1. Chichester, UK: John Wiley and Sons Ltd 17
- Raja S, Ganesan S, Sivakumar K, Thangaradjou T. (2010). Screening of marine actinobacteria for amylase enzymes inhibitors. Indian J Microbiol 50:233–7
- Ramkumar KM, Thayumanavan B, Palvannan T, Rajaguru P. (2010). Inhibitory effect of Gymnema Montanum leaves on α-glucosidase activity and α-amylase activity and their relationship with polyphenolic content. Med Chem Res 19:948–61
- Rawlings ND. (2010). Peptidase inhibitors in the MEROPS database. Biochimie 92:1463–83
- Roberts RM, Mathialagan N, Duffy JY, Smith GW. (1995). Regulation and regulatory role of proteinase inhibitors. Crit Rev Eukaryot Gene Expr 5:385–436
- Sakuda S, Isogai A, Matsumoto S, et al. (1986). The structure of allosamidin, a novel insect chitinase inhibitor, produced by Streptomyces sp. Tetrahedron Lett 27:2475–8
- Sakuda S, Isogai A, Makita T, et al. (1987). Structures of allisamidins, novel insect chitinase inhibitors, produced by Actinomycetes. Agri Biol Chem 51:3251–9
- Sathiyaseelan K, Stella D. (2012). Isolation and screening of α-glucosidase enzyme inhibitor producing marine actinobacteria isolated from Pichavaram mangrove. Int J Pharm Biol Archive 3:1142–9
- Seelmeier S, Schmidt H, Turk V, Von Der Helm K. (1988). Human immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A. Proc Nat Acad Sci 85:6612–16
- Seiberg M, Paine C, Sharlow E, et al. (2000a). Inhibition of melanosome transfer results in skin lightening. J Investigative Dermatol 115:162–7
- Seiberg M, Paine C, Sharlow E, et al. (2000b). The protease-activated receptor 2 regulates pigmentation via keratinocyte-melanocyte interactions. Ex Cell Res 254:25–32
- Skeggs L, Kahn J, Shumway N. (1957). The preparation and function of the angiotensin-converting enzyme. J Ex Med 103:295–9
- Sorimachi H, Ishiura S, Suzuki K. (1997). Structure and physiological function of calpains. Biochem J 328:721–32
- Suthindhiran KR, Jayasri M, Kannabiran K. (2009). α-glucosidase and α-amylase inhibitory activity of Micromonospora sp. VITSDK3 (EU551238). Int J Integrative Biol 6:115–20
- Takeuchi T, Ogawa K, Iinuma H, et al. (1973). Monoamine oxidase inhibitors isolated from fermented broths. J Antibiot 26:162–7
- Tews I, Terwisscha van Scheltinga AC, Perrakis A, et al. (1997). Substrate-assisted catalysis unifies two families of chitinolytic enzymes. J Am Chem Soc 119:7954–9
- Tobey NA, Hosseini SS, Caymaz-Bor C, et al. (2001). The role of pepsin in acid injury to esophageal epithelium. Am J Gastroenterol 96:3062–70
- Tokdar P, Ranadive P, Mascarenhas M, et al. (2011). A new pancreatic lipase inhibitor produced by a Streptomyces sp. MTCC 5219. Int Conference Life Sci Technol 3:7–10
- Tomita K, Oda N, Ohbayashi M, et al. (1990). A new screening method for melanin biosynthesis inhibitors using Streptomyces bikiniensis. J Antibiot 43:1601–5
- Truscheit E, Frommer W, Junge B, et al. (1981). Chemistry and biochemistry of microbial α-glucosidase inhibitors. Angew Chem Int Ed 20:744–61
- Tsuru D, Fujiwara K, Kunio K. (1978). Purification and characterization of L-pyrrolidonecarboxylate peptidase from Bacillus amyloliquefaciens. J Biochem 84:467–76
- Umezawa H. (1972). Enzyme inhibitors of microbial origin. Tokyo, Japan: University of Tokyo Press
- Umezawa H. (1982). Low-molecular-weight enzyme inhibitors of microbial origin. Ann Rev Microbiol 36:75–99
- Vernekar JV, Ghatge MS, Deshpande VV. (1999). Alkaline protease inhibitor: a novel class of antifungal proteins against phytopathogenic fungi. Biochem Biophy Res Commun 262:702–7
- Vértesy L, Oeding V, Bender R, et al. (1984). Tendamistat (HOE 467), a tight-binding α-amylase inhibitor from Streptomyces tendae 4158. Eur J Biochem 141:505–12
- Wang L, Hou Y, Peng J, et al. (2012). Bioactivity-based HPLC tandem Q/TOF for alpha-glucosidase inhibitors. Screening, identification, and quantification from Actinomycetes. Lat Am J Pharm 31:693–8
- Wehmeier U, Piepersberg W. (2004). Biotechnology and molecular biology of the α-glucosidase inhibitor acarbose. Appl Microbiol Biotechnol 63:613–25
- Weibel E, Hadvary P, Hochuli E, et al. (1987). Lipstatin, an inhibitor of pancreatic lipase, produced by Streptomyces toxytricini. I. Producing organism, fermentation, isolation and biological activity. J Antibiot 40:1081–5
- Yamamoto N. (1997). Antihypertensive peptides derived from food proteins. Peptide Sci 43:129–34
- Yamamoto N, Maeno M, Takano T. (1999). Purification and characterization of an antihypertensive peptide from a yogurt-like product fermented by Lactobacillus helveticus CPN4. J Dairy Sci 82:1388–93
- Yoon S-H, Robyt JF. (2003). Study of the inhibition of four alpha amylases by acarbose and its 4IV-α-maltohexaosyl and 4IV-α-maltododecaosyl analogues. Carbohyd Res 338:1969–80
- Zhu Y-P, Yin L-J, Cheng Y-Q, et al. (2008). Effects of sources of carbon and nitrogen on production of α-glucosidase inhibitor by a newly isolated strain of Bacillus subtilis B2. Food Chem 109:737–42